Toolkit/CIB1 N-terminal CRY2-binding region

CIB1 N-terminal CRY2-binding region

Protein Domain·Research·Since 2022

Also known as: CIB1, N-terminal region of the CRY2-binding domain of CIB1, N terminus of calcium and integrin-binding protein 1

Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

The CIB1 N-terminal CRY2-binding region is a protein domain derived from the N terminus of calcium and integrin-binding protein 1 (CIB1). It serves as the CIB1 partner in blue light-activated CRY2-CIB1 optogenetic dimerization systems.

Usefulness & Problems

Why this is useful

This domain is useful as a modular binding partner for CRY2 in blue light-responsive optogenetic systems. The supplied evidence specifically supports its use in a CRY2-CIB1 dimerization system developed for optogenetic control of PKC isozyme recruitment.

Source:

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

Problem solved

It helps solve the problem of coupling blue light input to inducible protein association through the CRY2-CIB1 interaction. In the cited application, this interaction was used to recruit individual PKC isozymes to the cell surface and promote specific phosphorylation of membrane proteins.

Source:

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

Problem links

Need precise spatiotemporal control with light input

Derived

The CIB1 N-terminal CRY2-binding region is a protein domain derived from the N terminus of calcium and integrin-binding protein 1 (CIB1). It is used as the CIB1 partner in blue light-activated CRY2-CIB1 optogenetic dimerization systems.

Need tighter control over gene expression timing or amplitude

Derived

The CIB1 N-terminal CRY2-binding region is a protein domain derived from the N terminus of calcium and integrin-binding protein 1 (CIB1). It is used as the CIB1 partner in blue light-activated CRY2-CIB1 optogenetic dimerization systems.

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Component: A low-level protein part used inside a larger architecture that realizes a mechanism.

Techniques

No technique tags yet.

Target processes

transcription

Input: Light

Implementation Constraints

cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment

The domain is described as the N terminus of the transcription factor calcium and integrin-binding protein 1 and specifically as the N-terminal region of the CRY2-binding domain of CIB1. The available evidence supports its implementation as a fusion-compatible partner in CRY2-CIB1 blue light optogenetic constructs, but does not provide construct architecture, expression system, or cofactor requirements.

The supplied evidence does not report the exact amino acid boundaries, kinetics, binding strength, or photophysical performance of the CIB1 N-terminal region. Validation in the provided material is limited to its identification as the N-terminal CRY2-binding region and its use in one optogenetic PKC recruitment system.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1tool developmentsupports2022Source 1needs review

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

Approval Evidence

1 source1 linked approval claimfirst-pass slug cib1-n-terminal-cry2-binding-region
the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1) (N-terminal region of the CRY2-binding domain of CIB1)

Source:

tool developmentsupports

The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.

Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)

Source:

Comparisons

Source-backed strengths

The evidence supports that this domain functions within a blue light-activated CRY2-CIB1 dimerization system. It was used in a tool designed to recruit PKC isozymes to the plasma membrane and drive specific phosphorylation of membrane proteins.

Compared with cryptochromes

CIB1 N-terminal CRY2-binding region and cryptochromes address a similar problem space because they share transcription.

Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Compared with Enhanced Magnets

CIB1 N-terminal CRY2-binding region and Enhanced Magnets address a similar problem space because they share transcription.

Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Compared with TAEL

CIB1 N-terminal CRY2-binding region and TAEL address a similar problem space because they share transcription.

Shared frame: same top-level item type; shared target processes: transcription; shared mechanisms: heterodimerization; same primary input modality: light

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    FoundationalSource 1Journal of Biological Chemistry2022Claim 1

    Derived from 1 linked claims. Example evidence: Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)